Biology:N-acetyl-D-glucosamine kinase
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Short description: Enzyme
 Generic protein structure example |
N-acetyl-D-glucosamine kinase is an enzyme that in humans is encoded by the NAGK gene.[1][2]
Function
N-acetylglucosamine kinase (NAGK; EC 2.7.1.59) converts endogenous N-acetylglucosamine (GlcNAc), a major component of complex carbohydrates, from lysosomal degradation or nutritional sources into GlcNAc 6-phosphate. NAGK belongs to the group of N-acetylhexosamine kinases and is a prominent salvage enzyme of amino sugar metabolism in mammals.[supplied by OMIM][2]
Interactions
NAGK has been shown to interact with STK16[3] and LNX1.[4]
References
- ↑ "Molecular cloning and characterization of murine and human N-acetylglucosamine kinase". European Journal of Biochemistry 267 (11): 3301–8. Jun 2000. doi:10.1046/j.1432-1327.2000.01360.x. PMID 10824116.
- ↑ 2.0 2.1 "Entrez Gene: NAGK N-acetylglucosamine kinase". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=55577.
- ↑ "Functional interaction between the Ser/Thr kinase PKL12 and N-acetylglucosamine kinase, a prominent enzyme implicated in the salvage pathway for GlcNAc recycling". The Journal of Biological Chemistry 277 (8): 6333–43. Feb 2002. doi:10.1074/jbc.M105766200. PMID 11741987.
- ↑ "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. Oct 2005. doi:10.1038/nature04209. PMID 16189514. Bibcode: 2005Natur.437.1173R.
Further reading
- "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1–2): 171–4. Jan 1994. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
- "N-acetylglucosamine kinase and N-acetylglucosamine 6-phosphate deacetylase in normal human erythrocytes and Plasmodium falciparum". British Journal of Haematology 95 (4): 645–53. Dec 1996. doi:10.1046/j.1365-2141.1996.d01-1955.x. PMID 8982040.
- "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1–2): 149–56. Oct 1997. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
- "Hexokinase isoenzymes in normal and cirrhotic human liver: suppression of glucokinase in cirrhosis". Biochimica et Biophysica Acta (BBA) - General Subjects 1379 (1): 134–42. Jan 1998. doi:10.1016/s0304-4165(97)00092-5. PMID 9468341.
- "Functional interaction between the Ser/Thr kinase PKL12 and N-acetylglucosamine kinase, a prominent enzyme implicated in the salvage pathway for GlcNAc recycling". The Journal of Biological Chemistry 277 (8): 6333–43. Feb 2002. doi:10.1074/jbc.M105766200. PMID 11741987.
- "Identification of the phosphotyrosine proteome from thrombin activated platelets". Proteomics 2 (6): 642–8. Jun 2002. doi:10.1002/1615-9861(200206)2:6<642::AID-PROT642>3.0.CO;2-I. PMID 12112843.
- "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides". Nature Biotechnology 21 (5): 566–9. May 2003. doi:10.1038/nbt810. PMID 12665801.
- "A protein interaction framework for human mRNA degradation". Genome Research 14 (7): 1315–23. Jul 2004. doi:10.1101/gr.2122004. PMID 15231747.
- "Use of a cell-free system to determine UDP-N-acetylglucosamine 2-epimerase and N-acetylmannosamine kinase activities in human hereditary inclusion body myopathy". Glycobiology 15 (11): 1102–10. Nov 2005. doi:10.1093/glycob/cwi100. PMID 15987957.
- "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. Oct 2005. doi:10.1038/nature04209. PMID 16189514. Bibcode: 2005Natur.437.1173R.
- "Structures of human N-Acetylglucosamine kinase in two complexes with N-Acetylglucosamine and with ADP/glucose: insights into substrate specificity and regulation". Journal of Molecular Biology 364 (3): 388–99. Dec 2006. doi:10.1016/j.jmb.2006.08.085. PMID 17010375.
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